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Issue 7, 2017
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In vivo activation of an [FeFe] hydrogenase using synthetic cofactors

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Abstract

[FeFe] hydrogenases catalyze the reduction of protons, and oxidation of hydrogen gas, with remarkable efficiency. The reaction occurs at the H-cluster, which contains an organometallic [2Fe] subsite. The unique nature of the [2Fe] subsite makes it dependent on a specific set of maturation enzymes for its biosynthesis and incorporation into the apo-enzyme. Herein we report on how this can be circumvented, and the apo-enzyme activated in vivo by synthetic active site analogues taken up by the living cell.

Graphical abstract: In vivo activation of an [FeFe] hydrogenase using synthetic cofactors

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Article information


Submitted
13 Jan 2017
Accepted
11 Apr 2017
First published
11 Apr 2017

This article is Open Access

Energy Environ. Sci., 2017,10, 1563-1567
Article type
Communication

In vivo activation of an [FeFe] hydrogenase using synthetic cofactors

N. Khanna, C. Esmieu, L. S. Mészáros, P. Lindblad and G. Berggren, Energy Environ. Sci., 2017, 10, 1563
DOI: 10.1039/C7EE00135E

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